Conformational features of polyglycine were evaluated. Polyglycine serves as a model of polypeptide backbones and several important biological structures (collagen, silk fibroin). A new structure of a polyglycine crystal has been determined based on molecular modeling and X-ray diffraction calculations. A paper was published. Performed amino acid sequence analysis of bacterial proteins having arrays of tandem repeats. Based on this analysis and molecular modeling, a beta-helix model was suggested for the filamentous hemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. A manuscript will be submitted for publication soon. Performed amino acid sequence analysis of signal peptides and regions adjacent to them in order to understand the mechanism of protein translocation across the cytoplasmic membrane. Established that the net charge of the first 18 residues of the mature sequence is essential for protein translocation of gram-negative bacteria. A manuscript will be submitted for publication soon. A short coiled-coil peptide with the potential to self-assemble into long fibrils has been designed, synthesized and analyzed. A manuscript is in preparation. - molecular modeling, protein structure, sequence analysis, tandem repeats